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- W2471002962 endingPage "636" @default.
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- W2471002962 abstract "Lipids are produced site-specifically in cells and then distributed nonrandomly among membranes via vesicular and nonvesicular trafficking mechanisms. The latter involves soluble amphitropic proteins extracting specific lipids from source membranes to function as molecular solubilizers that envelope their insoluble cargo before transporting it to destination sites. Lipid-binding and lipid transfer structural motifs range from multi-β-strand barrels, to β-sheet cups and baskets covered by α-helical lids, to multi-α-helical bundles and layers. Here, we focus on how α-helical proteins use amphipathic helical layering and bundling to form modular lipid-binding compartments and discuss the functional consequences. Preformed compartments generally rely on intramolecular disulfide bridging to maintain conformation (e.g., albumins, nonspecific lipid transfer proteins, saposins, nematode polyprotein allergens/antigens). Insights into nonpreformed hydrophobic compartments that expand and adapt to accommodate a lipid occupant are few and provided mostly by the three-layer, α-helical ligand-binding domain of nuclear receptors. The simple but elegant and nearly ubiquitous two-layer, α-helical glycolipid transfer protein (GLTP)-fold now further advances understanding." @default.
- W2471002962 created "2016-07-22" @default.
- W2471002962 creator A5022303540 @default.
- W2471002962 creator A5031949661 @default.
- W2471002962 creator A5077706769 @default.
- W2471002962 date "2017-06-20" @default.
- W2471002962 modified "2023-10-16" @default.
- W2471002962 title "How α-Helical Motifs Form Functionally Diverse Lipid-Binding Compartments" @default.
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